P2736
Pectinase from Aspergillus niger
aqueous solution
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form
aqueous solution
concentration
≥3000 units/mL
storage temp.
2-8°C
Application
Petctinase is an enzyme from Aspergillus niger that is used in plant protoplast preparation to digest cell wall prior to organelle isolation. It has been used to conduct partial saccharification of sugars. Pectinases are used to study their role in the invasion of plant tissues by phytopathogens, the spoilage of produce and various food processing and plant biotechnology applications.
Biochem/physiol Actions
Pectolytic enzyme preparation produced from a selected strain of Aspergillus niger: contains mainly pectintranseliminase, polygalacturonase, and pectinesterase and small amounts of hemicellulases and cellulases. Pectinases hydrolyses pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. It is a source of pectinase activity, also containing cellulase and hemicellulase activities.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Legal Information
A product of Novozyme Corp.
Pectinex is a registered trademark of Novozymes Corp.
replaced by
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
新产品
Certificates of Analysis (COA)
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Meredith C Edwards et al.
Applied and environmental microbiology, 77(15), 5184-5191 (2011-06-15)
Ethanologenic Escherichia coli strain KO11 was sequentially engineered to contain the Klebsiella oxytoca cellobiose phosphotransferase genes (casAB) as well as a pectate lyase (pelE) from Erwinia chrysanthemi, yielding strains LY40A (casAB) and JP07 (casAB pelE), respectively. To obtain an effective
Indra Prakash et al.
International journal of molecular sciences, 13(11), 15126-15136 (2012-12-04)
Catalytic hydrogenation of rebaudioside B, rebaudioside C, and rebaudioside D; the three ent-kaurane diterpene glycosides isolated from Stevia rebaudiana was carried out using Pd(OH)(2). Reduction of steviol glycosides was performed using straightforward synthetic chemistry with the catalyst Pd(OH)(2) and structures
Sara Posé et al.
Journal of experimental botany, 64(12), 3803-3815 (2013-07-23)
Antisense-mediated down-regulation of the fruit-specific polygalacturonase (PG) gene FaPG1 in strawberries (Fragaria×ananassa Duch.) has been previously demonstrated to reduce fruit softening and to extend post-harvest shelf life, despite the low PG activity detected in this fruit. The improved fruit traits
Ding-Tao Wu et al.
Carbohydrate polymers, 97(2), 398-405 (2013-08-06)
Polysaccharides from Ganoderma spp. and their adulterants were firstly investigated and compared using saccharide mapping, enzymatic (endo-1,3-β-D-glucanase and pectinase) digestion followed by polysaccharide analysis using carbohydrate gel electrophoresis analysis. The results showed that both 1,3-β-D-glucosidic and 1,4-α-D-galactosiduronic linkages were existed
Joan Ho-Huu et al.
BMC evolutionary biology, 12, 195-195 (2012-10-03)
Gene duplications are a molecular mechanism potentially mediating generation of functional novelty. However, the probabilities of maintenance and functional divergence of duplicated genes are shaped by selective pressures acting on gene copies immediately after the duplication event. The ratio of
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